期刊
CRYOBIOLOGY
卷 60, 期 1, 页码 91-99出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.cryobiol.2009.07.005
关键词
Hydrophobic effect; Thermodynamics; Clathrate cages; Hydrate cages; Cold denaturation; Proteins
资金
- Natural Sciences and Engineering Research Council of Canada
- le Fonds Quebecois de la recherche sur la nature et les technologies
- Academy of Finland through its COMP Center of Excellence and TransPoly
The hydrophobic effect is considered the main driving force for protein folding and plays an important role in the stability of those biomolecules. Cold denaturation, where the native state of the protein loses its stability upon cooling, is also attributed to this effect. It is therefore not surprising that a lot of effort has been spent in understanding this phenomenon. Despite these efforts, many unresolved fundamental aspects remain. In this paper we review and summarize the thermodynamics of proteins, the hydrophobic effect and cold denaturation. We start by accounting for these phenomena macroscopically then move to their atomic-level description. We hope this review will help the reader gain insights into the role played by the hydrophobic effect in cold denaturation. (C) 2009 Elsevier Inc. All rights reserved.
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